| Applications | WB, IP |
| Clone | 580223 |
| Clonality | Monoclonal |
| Host | Mouse |
| Conjugate | Alexa Fluor 647 |
| Immunogen | E. coli-derived recombinant C. botulinum BoNT-C1 Heavy Chain Asn866-Glu1291 Accession # P18640 |
| Specificity | Detects C. botulinum BoNT-C1 Heavy Chain in direct ELISAs. In direct ELISAs, no cross-reactivity with the Light Chains of BoNT-A, -B, -C1, -D, -E, -F, -G, or Heavy Chains of BoNT-D or -G is observed. |
| Isotype | IgG1 |
| Clonality | Monoclonal |
| Host | Mouse |
| Purity Statement | Protein A or G purified |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Storage | Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied |
| Buffer | Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide |
BoNT-C1 (Botulinum neurotoxin C1 [heavy chain]) is a 100 kDa C-terminal fragment of the C1 Clostridum botulinum neurotoxin (holo)precursor. It constitutes a nonenzymatic part of a Zn2+-dependent M27 family endoprotease that potently blocks neurosecretion. The inactive 1291 amino acid (aa), 150 kDa C1 precursor is cleaved between Lys449Thr450 to generate a heterodimeric toxin held together by a preexisting interchain disulfide bond between Cys437 and Cys453. The 100 kDa C-terminus (heavy chain) acts as a ligand for neuronal membrane ecto-acceptors, inducing its translocation and internalization. The 50 kDa N-terminal light chain acts as an intracellular peptidase that cleaves SNAP-25 and syntaxin. This is suggested to block noradrenalin release from a readily releasable pool of vesicles. Over aa 866-1291, the C1 heavy chain shares less than 40% aa identity with the D-type neurotoxin heavy chain.
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